alpha-xylosidase [Escherichia coli].

LOCUS       WP_000702966             772 aa            linear   BCT 10-DEC-2019
ACCESSION   WP_000702966
VERSION     WP_000702966.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Kitamura,M., Ose,T., Okuyama,M., Watanabe,H., Yao,M., Mori,H.,
            Kimura,A. and Tanaka,I.
  TITLE     Crystallization and preliminary X-ray analysis of alpha-xylosidase
            from Escherichia coli
  JOURNAL   Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (Pt 2),
            178-179 (2005)
   PUBMED   16510986
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Lovering,A.L., Lee,S.S., Kim,Y.W., Withers,S.G. and Strynadka,N.C.
  TITLE     Mechanistic and structural analysis of a family 31
            alpha-glycosidase and its glycosyl-enzyme intermediate
  JOURNAL   J. Biol. Chem. 280 (3), 2105-2115 (2005)
   PUBMED   15501829
REFERENCE   3  (residues 1 to 772)
  AUTHORS   Okuyama,M., Mori,H., Chiba,S. and Kimura,A.
  TITLE     Overexpression and characterization of two unknown proteins, YicI
            and YihQ, originated from Escherichia coli
  JOURNAL   Protein Expr. Purif. 37 (1), 170-179 (2004)
   PUBMED   15294295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF007940.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10658
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..772
                     /gene="yicI"
     Protein         1..772
                     /product="alpha-xylosidase"
                     /EC_number="3.2.1.177"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=87783
     Region          1..666
                     /region_name="PRK10658"
                     /note="putative alpha-glucosidase; Provisional"
                     /db_xref="CDD:236731"
ORIGIN      
        1 mkisdgnwli qpglnlihpl qvfeveqqgn emvvyaaprd vrertwqldt plftlrffsp
       61 qegivgvrie hfqgalnngp hyplnilqdv kvtientery aefksgnlsa rvskgefwsl
      121 dflrngerit gsqvknngyv qdtnnqrnym ferldlgvge tvyglgerft alvrngqtve
      181 twnrdggtst eqayknipfy mtnrgygvlv nhpqcvsfev gsekvskvqf sveseyleyf
      241 vidgptpkav ldrytrftgr palppawsfg lwlttsfttn ydeatvnsfi dgmagrnlpl
      301 hvfhfdcfwm kafqwcdfew dpltfpdpeg mirrlkakgl kicvwinpyi gqkspvfkel
      361 qekgyllkrp dgslwqwdkw qpglaiydft npdackwyad klkglvamgv dcfktdfger
      421 ipidvqwfdg sdpqkmhnhy ayiynelvwn vlkdtvgeee avlfarsasv gaqkfpvhwg
      481 gdcyanyesm aeslrgglsi glsgfgfwsh diggfental ahvykrwcaf gllsshsrlh
      541 gsksyrvpwa yddescdvvr fftqlkcrmm pylyreaara nargtpmmra mmmefpddpa
      601 cdyldrqyml gdnvmvapvf seagdvqfyl pegrwthlwh ndeldgsrwh kqqhsflslp
      661 vyvrdntlla lgnneqrpdy awhegtafql fnlqdgheai cevpaadgsv lftlkaartg
      721 ntitvtgage aknwtlclrn ivkvnglqgg sqaeseqglv vtpqgnalti tl